A stable, high relaxivity, diaqua gadolinium complex that suppresses anion and protein binding

Dimitri Messeri; Mark P. Lowe; David Parker; Mauro Botta

doi:10.1039/b108294a

A stable, high relaxivity, diaqua gadolinium complex that suppresses anion and protein binding

Dimitri Messeri
, Mark P. Lowe
, David Parker
, Mauro Botta

Dipartimento di Scienze e Innovazione Tecnologica

Risultato della ricerca: Contributo su rivista › Articolo in rivista › peer review

Abstract

The high relaxivity of [GdaDO3A]³⁻ (r_1p = 12.3 mM^-1 s^-1, 20 MHz, 298 K, τ_m = 30 ns) in water is maintained in serum solution because the binding of protein and endogeneous anions, e.g. HCO₃⁻/CO₃²⁻ is suppressed by electrostatic repulsion.

Lingua originale	Inglese
pagine (da-a)	2742-2743
Numero di pagine	2
Rivista	Chemical Communications
Volume	1
Numero di pubblicazione	24
DOI	https://doi.org/10.1039/b108294a
Stato di pubblicazione	Pubblicato - 2001

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10.1039/b108294a

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@article{79b9753671114285901f42dcb0802153,

title = "A stable, high relaxivity, diaqua gadolinium complex that suppresses anion and protein binding",

abstract = "The high relaxivity of [GdaDO3A]3− (r1p = 12.3 mM-1 s-1, 20 MHz, 298 K, τm = 30 ns) in water is maintained in serum solution because the binding of protein and endogeneous anions, e.g. HCO3−/CO32− is suppressed by electrostatic repulsion.",

author = "Dimitri Messeri and Lowe, \{Mark P.\} and David Parker and Mauro Botta",

year = "2001",

doi = "10.1039/b108294a",

language = "English",

volume = "1",

pages = "2742--2743",

journal = "Chemical Communications",

issn = "1359-7345",

publisher = "Royal Society of Chemistry",

number = "24",

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TY - JOUR

T1 - A stable, high relaxivity, diaqua gadolinium complex that suppresses anion and protein binding

AU - Messeri, Dimitri

AU - Lowe, Mark P.

AU - Parker, David

AU - Botta, Mauro

PY - 2001

Y1 - 2001

N2 - The high relaxivity of [GdaDO3A]3− (r1p = 12.3 mM-1 s-1, 20 MHz, 298 K, τm = 30 ns) in water is maintained in serum solution because the binding of protein and endogeneous anions, e.g. HCO3−/CO32− is suppressed by electrostatic repulsion.

AB - The high relaxivity of [GdaDO3A]3− (r1p = 12.3 mM-1 s-1, 20 MHz, 298 K, τm = 30 ns) in water is maintained in serum solution because the binding of protein and endogeneous anions, e.g. HCO3−/CO32− is suppressed by electrostatic repulsion.

UR - https://www.scopus.com/pages/publications/0035930740

U2 - 10.1039/b108294a

DO - 10.1039/b108294a

M3 - Article

AN - SCOPUS:0035930740

SN - 1359-7345

VL - 1

SP - 2742

EP - 2743

JO - Chemical Communications

JF - Chemical Communications

IS - 24

ER -

A stable, high relaxivity, diaqua gadolinium complex that suppresses anion and protein binding

Abstract

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